› 4y5g

X-ray diffraction
1.47Å resolution

Endothiapepsin in complex with fragment 272

Released:
DOI: 10.2210/pdb4y5g/pdb
PDB entry 4y5g coloured by chain, front view.
PDB entry 4y5g coloured by chain, side view.
PDB entry 4y5g coloured by chain, top view.
Source organism: Cryphonectria parasitica
Entry authors: Wang X, Heine A, Klebe G

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothiapepsin Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 33.81 KDa
Source organism: Cryphonectria parasitica
UniProt:
  • Canonical: P11838 (Residues: 90-419; Coverage: 83%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

4 bound ligands:
Ligand 47U 1 x 47U
Ligand GOL 1 x GOL
Ligand ACT 1 x ACT
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 45.402Å b: 73.145Å c: 52.869Å
α: 90° β: 109.65° γ: 90°
R-values:
R R work R free
0.124 0.123 0.156

Quick links